4RYB

Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Neisseria meningitidis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
A	0005737	cellular_component	cytoplasm
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0033818	molecular_function	beta-ketoacyl-acyl-carrier-protein synthase III activity
B	0003824	molecular_function	catalytic activity
B	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
B	0005737	cellular_component	cytoplasm
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0033818	molecular_function	beta-ketoacyl-acyl-carrier-protein synthase III activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 401

Chain	Residue
B	ARG61
B	ASP65
B	ASP70
B	SER71

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 402

Chain	Residue
B	GLN240

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Region: {"description":"ACP-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_01815","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01815","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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